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P48845 (DEXT_PENMI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dextranase
EC=3.2.1.11
Alternative name(s):
Alpha-1,6-glucan-6-glucanohydrolase
Gene names
Name:DEX
OrganismPenicillium minioluteum (Filamentous fungus) (Talaromyces minioluteus)
Taxonomic identifier28574 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Talaromyces

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.

Subcellular location

Secreted.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 49 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondextranase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 3415
PRO_0000012213
Chain35 – 608574Dextranase
PRO_0000012214

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential

Secondary structure

1 ................................................................................................................... 608
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48845 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 6309B5FB372D381D

FASTA60865,961
        10         20         30         40         50         60 
MATMLKLLAL TLAISESAIG AVMHPPGNSH PGTHMGTTNN THCGADFCTW WHDSGEINTQ 

        70         80         90        100        110        120 
TPVQPGNVRQ SHKYSVQVSL AGTNNFHDSF VYESIPRNGN GRIYAPTDPP NSNTLDSSVD 

       130        140        150        160        170        180 
DGISIEPSIG LNMAWSQFEY SHDVDVKILA TDGSSLGSPS DVVIRPVSIS YAISQSDDGG 

       190        200        210        220        230        240 
IVIRVPADAN GRKFSVEFKT DLYTFLSDGN EYVTSGGSVV GVEPTNALVI FASPFLPSGM 

       250        260        270        280        290        300 
IPHMTPDNTQ TMTPGPINNG DWGAKSILYF PPGVYWMNQD QSGNSGKLGS NHIRLNSNTY 

       310        320        330        340        350        360 
WVYLAPGAYV KGAIEYFTKQ NFYATGHGIL SGENYVYQAN AGDNYIAVKS DSTSLRMWWH 

       370        380        390        400        410        420 
NNLGGGQTWY CVGPTINAPP FNTMDFNGNS GISSQISDYK QVGAFFFQTD GPEIYPNSVV 

       430        440        450        460        470        480 
HDVFWHVNDD AIKIYYSGAS VSRATIWKCH NDPIIQMGWT SRDISGVTID TLNVIHTRYI 

       490        500        510        520        530        540 
KSETVVPSAI IGASPFYASG MSPDSRKSIS MTVSNVVCEG LCPSLFRITP LQNYKNFVVK 

       550        560        570        580        590        600 
NVAFPDGLQT NSIGTGESII PAASGLTMGL NISNWTVGGQ KVTMENFQAN SLGQFNIDGS 


YWGEWQIS

« Hide

References

[1]"Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris."
Roca H., Garcia B.M., Rodriguez E., Mateu D., Coroas L., Cremata J.A., Garcia R., Pons T., Delgado J.
Yeast 12:1187-1200(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-50.
Strain: Sp. Dierckx / MUCL 38929.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L41562 Genomic DNA. Translation: AAB47720.1.
PIRS72177.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OGMX-ray1.80X36-608[»]
1OGOX-ray1.65X36-608[»]
ProteinModelPortalP48845.
SMRP48845. Positions 37-608.
ModBaseSearch...

Protein family/group databases

CAZyGH49. Glycoside Hydrolase Family 49.
mycoCLAPDEX49A_PENMI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.160.20.10. 1 hit.
2.60.350.10. 1 hit.
InterProIPR005192. Glyco_hydro_49.
IPR023226. Glyco_hydro_49_N_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamPF03718. Glyco_hydro_49. 1 hit.
[Graphical view]
SUPFAMSSF101596. Glyco_hydro_49_N. 1 hit.
SSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP48845.

Entry information

Entry nameDEXT_PENMI
AccessionPrimary (citable) accession number: P48845
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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